Abstract
Although the biochemistry of early trimming reactions by glucosidases and ER mannosidases occurring on asparagine-linked oligosaccharides has been known for a long time, their involvement in quality control of protein folding has become apparent only more recently. Here we review the evidence for the involvement of specific oligosaccharide trimming intermediates such as Glc(1)Man(9)GlcNAc(2) and Man(8)GlcNAc(2) B isomer in this fundamental cellular process and the subcellular distribution of components of the protein quality control machinery which indicates the involvement of both the ER and pre-Golgi intermediates in this process. In addition, recent studies on the subcellular distribution of endomannosidase in conjunction with previously obtained biochemical data will be reviewed which demonstrate that an alternative deglucosylation pathway exists in pre-Golgi intermediates and the Golgi apparatus.
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